Tyrosinase was immobilized on magnetite using amino groups from an enzyme for the purpose of finding means for removing phenols from wastewater. This immobilization noticeably improved storage and operational stabilities, due possibly to elimination of reactions of amino groups in tyrosinase with quinones formed by oxidation of phenols. The oxidation of substituted phenols with magnetite-immobilized tyrosinase was dependent on substituent groups and their positions. P ASubstituted phenols were better substrates than o and m substituted phenols.

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